Dr. Harm H. Kampinga

Dept. Biomedical Sciences, UMCG/RuG, Groningen, The Netherlands

Invited by Dr. Valérie Mezger

“Collapse of protein homeostasis as driver of age-related protein aggregation diseases“

The seminar will take place in the Institut Jacques Monod seminar room (RB-18B).

Bâtiment Buffon, 15 rue Hélène Brion, Paris 13^th.

On Wednesday, April 15^that 11:00 am.

Harm’s research has always been related cellular responses to the protein un-or misfolding on cellular functions. Initially, this research was centred around the biological effects of heat shock on cells in relation to the use of hyperthermia in cancer treatments. In more recent years, his research focused on the understanding of the functioning and regulation (by cofactors) of the diverse chaperone machines in living mammalian cells in protein quality control (folding, proteaosmal or autophagosomal degradation) and on how these functions or dysfunctions of heat shock proteins may play a role in the cause of human diseases, or may be used to antagonise the onset or progression of particular neurodegenerative diseases such as Huntington’s disease, and of cellular ageing in general. Ongoing projects include the regulation of input and output (fate) of clients in and from the Hsp70 machine, the structure and function of the J-domain protein, DNAJB6 as strong inhibitor of amyloidogenesis, the unravelling mechanisms of chaperonopathies, diseases caused by mutations in chaperones, and studying the importance of imbalances in protein homeostasis for cellular aging.

Relevant publications from the speaker:

• Wentink et al., Mechanisms and regulation of the Hsp70 chaperone network. Nat Rev Mol Cell Biol. 2026, 27(2):110-128
• Mauthe et al., A chaperone-proteasome-based fragmentation machinery is essential for aggrephagy. Nat Cell Biol. 2025, 27(9):1448-1464
• Korsten et al., Nuclear poly-glutamine aggregates rupture the nuclear envelope and hinder its repair. J Cell Biol. 2024; 223(11):e202307142.
• Kuiper et al., The chaperone DNAJB6 surveils FG-nucleoporins and is required for interphase nuclear pore complex biogenesis. Nat Cell Biol. 2022, 24(11):1584-1594
• Huiting et al., Targeting DNA topoisomerases or checkpoint kinases results in an overload of chaperone systems, triggering aggregation of a metastable subproteome. 2022, 11:e70726.
• Thiruvalluvan et al., DNAJB6, a Key Factor in Neuronal Sensitivity to Amyloidogenesis. Mol Cell. 2020,78(2):346-358.
• Kakkar V et al., The S/T-Rich Motif in the DNAJB6 Chaperone Delays Polyglutamine Aggregation and the Onset of Disease in a Mouse Model. Mol Cell. 2016, 62(2):272-283.
• Vos et al., Specific protein homeostatic functions of small heat-shock proteins increase lifespan. Aging Cell. 2016, 15(2):217-226.
• Vos et al., HSPB7 is the most potent polyQ aggregation suppressor within the HSPB family of molecular chaperones. Hum Mol Genet. 2010, 19(23):4677-4693.
• Hageman et al., A DNAJB chaperone subfamily with HDAC-dependent activities suppresses toxic protein aggregation. Mol Cell. 2010, 37(3):355-69.